Literature summary extracted from
Uehara, R.; Angkawidjaja, C.; Koga, Y.; Kanaya, S.
Formation of the high-affinity calcium binding site in pro-subtilisin E with the insertion sequence IS1 of pro-Tk-subtilisin (2013), Biochemistry, 52, 9080-9088.
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.4.21.B57 |
Ca2+ |
bound at the high-affinity Ca1 site and low-affinity Ca2 site |
Thermococcus kodakarensis |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.B57 |
Thermococcus kodakarensis |
P58502 |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.4.21.B57 |
proteolytic modification |
autocatalytic processing, pro-Tk-subtilisin from Thermococcus kodakarensis is fully folded, because it does not require the structural rearrangement upon autoprocessing for the formation of the Ca2+-binding Ca1 site due to the presence of the insertion sequence IS1 between the propeptide and subtilisin domains |
Thermococcus kodakarensis |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.21.B57 |
Tk-subtilisin |
- |
Thermococcus kodakarensis |